Cell Signaling Technology

Product Pathways - Protein Stability

CAND1 (D1F2) Rabbit mAb #8759

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M R Mk (C) (Dg) (Pg) (GP) Endogenous 130 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  C=Chicken  Dg=Dog  Pg=Pig  GP=Guinea Pig
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

CAND1 (D1F2) Rabbit mAb recognizes endogenous levels of total CAND1 protein. Based upon sequence alignment, this antibody is not predicted to cross-react with CAND2/TIP120B.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala561 of human CAND1 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, either mock transfected (-) or transfected with a Myc-tagged cDNA expression construct encoding full-length human CAND1 (hCAND1-Myc, +), using CAND1 (D1F2) Rabbit mAb.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using CAND1 (D1F2) Rabbit mAb.

Background

Cullin-associated and neddylation-dissociated (CAND1)/TIP120A is a protein containing multiple HEAT repeats. It functions, in part, as an inhibitor of multiple cullin-RING ubiquitin ligases (CRLs) via binding to cullin-RBX complexes that are both unconjugated to NEDD8 and lack association with substrate recognition subunits (1-3). Indeed, CAND1 has been shown to bind all cullin family members in human cells and analysis of the crystal structure of human CAND1 bound to the CUL1-RBX1 complex suggests that CAND1 inhibits the activity of CRLs by sterically blocking both the substrate recognition subunit binding site and the NEDD8 conjugation site (1,3,4). Conversely, CAND1 binding to cullin-RBX complexes is incompatible with neddylation as NEDD8 conjugated to cullins blocks CAND1 binding, suggesting that CAND1 binds to cullins only after the COP9 signalosome has catalyzed cullin deneddylation. Through its ability to negatively regulate CRL assembly, CAND1 plays an integral part in facilitating CRL activation cycles that allow CRLs to utilize distinct substrate recognition subunits and protects these subunits from undergoing ubiquitin-dependent degradation (5-7).

  1. Liu, J. et al. (2002) Mol Cell 10, 1511-8.
  2. Zheng, J. et al. (2002) Mol Cell 10, 1519-26.
  3. Min, K.W. et al. (2003) J Biol Chem 278, 15905-10.
  4. Goldenberg, S.J. et al. (2004) Cell 119, 517-28.
  5. Wee, S. et al. (2005) Nat Cell Biol 7, 387-91.
  6. Wu, J.T. et al. (2005) Nat Cell Biol 7, 1014-20.
  7. Cope, G.A. and Deshaies, R.J. (2006) BMC Biochem 7, 1.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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